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Molecular Immunology > Antigen recognition (6) > Flashcards

Antigen recognition (6) Flashcards

1
Q

What does the immune system recognise?

A
  1. Non self molecules (antigens)

2. Danger

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2
Q

Where are danger signals generated from?

A

From injured tissues endogenously.

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3
Q

Who came up with the danger hypothesis in 1994?

A

Matzinger.

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4
Q

What happens after primary contact with an antigen?

A

An innate and a weak adaptive response

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5
Q

What does secondary contact with an antigen result in?

A

An enhanced adaptive response resulting in immunological memory.

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6
Q

What leucocytes are involved in the innate response?

A

Phagocytes, NK cells.

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7
Q

What leucocytes are involved in the adaptive response?

A

B and T lymphocytes.

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8
Q

What soluble factors are involved in the innate response?

A

Lysosyme, complement and interferons.

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9
Q

What soluble factors are involved in the adaptive response?

A

Antibodies.

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10
Q

What is clonal selection?

A

When T and B lymphocytes with the correct receptor undergo……..

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11
Q

What can persist after an infection?

A

T and B memory cells.

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12
Q

Who came up with the Clonal Selection Hypothesis in 1958?

A

Macfarlane Burnett.

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13
Q

What does the clonal selection hypothesis say happens early on in development?

A

Lymphocytes that recognise ‘self’ are detected early in development.

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14
Q

What happens in the clonal selection hypothesis after lymphocytes that recognise ‘self’ are deleted?

A

The lymphocyte with the appropriate receptor expand to produce both plasma cells and memory cells. These plasma cells go on to produce antibody.

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15
Q

What happens in the primary lymphoid tissue?

A

Lymphocytes reach maturity.

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16
Q

What happens in the secondary lymphoid tissue?

A

Mature lymphocytes are stimulated by antigen.

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17
Q

What happens in the draining lymph node?

A

Activation of the adaptive immune response?

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18
Q

How does the bacterial component reach the lymph node and how?

A

Through the afferent lymphatic vessel via dendritic cells.

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19
Q

What activates the T cells in the lymph node?

A

Dendritic cells.

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20
Q

How do naive T/B cells reach the lymph node?

A

Through the artery.

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21
Q

What leaves the lymph node through the efferent lymphatic vessel?

A

Antibodies and effector T cells.

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22
Q

What is an epitope?

A

The molecular shape an antibody recognizes on an antigen.

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23
Q

What two forms of antibody (immunogloblins) are there?

A
  1. Integral membrane proteins on B lymphocytes.

2. Soluble proteins secreted by plasma cells.

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24
Q

What are antigen receptors?

A

Antibodies existing on integral membrane proteins on B lymphocytes.

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25
Q

What are antigen eliminators?

A

Antibodies existing as soluble proteins secreted by plasma cells.

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26
Q

Antibodies structure reflect their dual roles. What are these two roles?

A

1, Antigen recognition.

2. Antigen elimination.

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27
Q

What part of the antibody is used for antigen recognition?

A

Fab regions.

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28
Q

What part of the antibody is used for antigen elimination?

A

Fc region.

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29
Q

Why can the Fab regions be involved in antigen recognition?

A

They are variable in sequence so can bind antigens specifically.

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30
Q

Why can the Fc regions be involved in antigen elimination?

A

They are constant in sequence so can bind to Fc receptors on various immune system cells.

31
Q

Fc regions on antibodies can bind to Fc receptors on immune system cells in order to undergo antigen elimination. What cells have these receptors?

A

Phagocytes and NK cells.

32
Q

How heavy is the light chain?

A

25kD

33
Q

How heavy is the heavy chain?

A

50kD

34
Q

How heavy is an immuogloblin?

A

150kd.

35
Q

Only the Fab fragment is commonly used in research. True or false?

A

False, the Fc fragment can be used also.

36
Q

What antibody fragments are produced by papain proteolytic cleavage?

A

Fab, Fab, Fc.

37
Q

What antibody fragments are produced by pepsin proteolytic cleavage?

A

F(ab’)2

38
Q

What do the immunoglobulin classes differ in?

A

Amino acid sequences of their heavy chains.

39
Q

What is the other name for IgG?

A

γ

40
Q

What is the other name for IgM?

A

μ

41
Q

What is the other name for IgA?

A

α

42
Q

What is the other name for IgD?

A

δ

43
Q

What is the other name for IgE?

A

ε

44
Q

What is the main role of IgG?

A

Secondary responses.

45
Q

What is the main role of IgM?

A

Primary responses

46
Q

What is the main role of IgA?

A

Protects mucosal surfaces

47
Q

What is the main role of IgD?

A

Do not know.

48
Q

What is the main role of IgG?

A

Allergy.

49
Q

What immunogloblin class is present at very low levels?

A

E.

50
Q

What is the main class of antibddy in serum?

A

G.

51
Q

Further information on the structure of antibodies came from protein sequencing of which proteins?

A

Myeloma proteins.

52
Q

Are the L chain types kappa and lambda class restricted?

A

No.

53
Q

Are constant regions the same for a given H chain class or L chain type?

A

Yes.

54
Q

What types of domains are antibodies comprised of?

A

Homologous domains.

55
Q

How many amino acids comprise the immunogloblin domain?

A

110.

56
Q

What is found in the immunogloblin domain allowing the structure to be compact?

A

Disulphide bridge.

57
Q

The immunogloblin fold has a different amount of beta strands depending on whether it is in the C or V domain. How many beta strands are in the immungloblin fold when it is in the C and V domain respectively?

A

7 in the constant, 9 in the variable.

58
Q

How many members are there in the Immunoglobulin gene superfamily in the human genome?

A

765 members.

59
Q

What three things is the immunogloblin gene superfamily involved in?

A

Recognition, binding and adhesion.

60
Q

How many hypervariable regions are in the variable regions of antibodies

A

3.

61
Q

How long are hypervariable regions in antibodies?

A

7-12 amino acids.

62
Q

What can hypervariable regions also be known as?

A

CDR’s (complementary determining regions).

63
Q

The variable region in the antibodies are made up of two regions. What are these?

A

The hypervariable and the framework regions.

64
Q

What type of interaction forms between the antibody and the antigens?

A

Non-covalent. These include electrostatic interactions, hydrogen bonds, VDW forces, hydrophobic interactions.

65
Q

The non covalent interactions between an antibody and antigen are individually weak. When are they strong?

A

When many are formed simultaneously due to the site and the antigen containing complementary residues. This results in the antibody and antigen interaction being specific and at high affinity.

66
Q

What do surface membrane immunogloblins contain?

A

26 hydrophobic amino acids at the C terminal.

67
Q

What Ig classes can serve as B cell receptors?

A

All of them.

68
Q

All classes of Ig can serve as B cell receptors. What two classes are mainly expressed by B cells?

A

M and D.

69
Q

B cell receptors can recognize and bind to antigen. What can they not do?

A

Generate a signal.

70
Q

What proteins are membrane bound immunoglobins also associated with?

A

Igalpha and Igbeta.

71
Q

What do Igalpha and Igbeta contain?

A

A single ITAM

72
Q

Where are the ITAMS in Igalpha and Igbeta

A

In the long cytoplasmic domains.

73
Q

How do Ig alpha and Igbeta arrange themselves around the B cell receptor?

A

As alpha/beta dimer on either side.

Molecular Immunology (9 decks)

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